메뉴 건너뛰기




Volumn 64, Issue 6, 2013, Pages 1553-1564

Lamin-like analogues in plants: The characterization of NMCP1 in Allium cepa

Author keywords

Allium cepa; bioinformatics analysis; immunoelectron microscopy; immunofluorescence microscopy; LINC proteins; NMCP1 proteins; nucleoskeleton; phylogenetic analysis; plamina; plant lamina; protein analysis.

Indexed keywords

NUCLEAR PROTEIN; VEGETABLE PROTEIN;

EID: 84876060083     PISSN: 00220957     EISSN: 14602431     Source Type: Journal    
DOI: 10.1093/jxb/ert020     Document Type: Article
Times cited : (56)

References (37)
  • 2
    • 44049093545 scopus 로고    scopus 로고
    • Quantitation of protein in samples prepared for 2-D electrophoresis
    • Berkelman T. 2008. Quantitation of protein in samples prepared for 2-D electrophoresis. Methods in Molecular Biology 424, 43-49.
    • (2008) Methods in Molecular Biology , vol.424 , pp. 43-49
    • Berkelman, T.1
  • 3
    • 1942487278 scopus 로고    scopus 로고
    • Biochemical and immunological characterization of pea nuclear intermediate filament proteins
    • Blumenthal SS, Clark GB, Roux SJ. 2004. Biochemical and immunological characterization of pea nuclear intermediate filament proteins. Planta 218, 965-975.
    • (2004) Planta , vol.218 , pp. 965-975
    • Blumenthal, S.S.1    Clark, G.B.2    Roux, S.J.3
  • 7
    • 0035999986 scopus 로고    scopus 로고
    • An HMM model for coiled-coil domains and a comparison with PSSM-based predictions
    • Delorenzi M, Speed T. 2002. An HMM model for coiled-coil domains and a comparison with PSSM-based predictions. Bioinformatics 18, 617-625.
    • (2002) Bioinformatics , vol.18 , pp. 617-625
    • Delorenzi, M.1    Speed, T.2
  • 10
    • 84858966521 scopus 로고    scopus 로고
    • NUP-1 is a large coiled-coil nucleoskeletal protein in trypanosomes with lamin-like functions
    • Dubois KN, Alsford S, Holden JM, et al.. 2012. NUP-1 is a large coiled-coil nucleoskeletal protein in trypanosomes with lamin-like functions. PLoS Biology 10, e1001287.
    • (2012) PLoS Biology , vol.10
    • Dubois, K.N.1    Alsford, S.2    Holden, J.M.3
  • 12
    • 67649703990 scopus 로고    scopus 로고
    • Nuclear envelope and nuclear pore complex structure and organization in tobacco BY-2 cells
    • Fiserova J, Kiseleva E, Goldberg MW. 2009. Nuclear envelope and nuclear pore complex structure and organization in tobacco BY-2 cells. The Plant Journal 59, 243-255.
    • (2009) The Plant Journal , vol.59 , pp. 243-255
    • Fiserova, J.1    Kiseleva, E.2    Goldberg, M.W.3
  • 14
    • 84856585935 scopus 로고    scopus 로고
    • Phytozome: A comparative platform for green plant genomics
    • Goodstein DM, Shu S, Howson R et al.. 2012. Phytozome: a comparative platform for green plant genomics. Nucleic Acids Research 40, D1178-D1186.
    • (2012) Nucleic Acids Research , vol.40
    • Goodstein, D.M.1    Shu, S.2    Howson, R.3
  • 15
    • 72749086154 scopus 로고    scopus 로고
    • Characterization of SUN-domain proteins at the higher plant nuclear envelope
    • Graumann K, Runions J, Evans DE. 2010. Characterization of SUN-domain proteins at the higher plant nuclear envelope. The Plant Journal 61, 134-144.
    • (2010) The Plant Journal , vol.61 , pp. 134-144
    • Graumann, K.1    Runions, J.2    Evans, D.E.3
  • 18
    • 77953292796 scopus 로고    scopus 로고
    • Differential nuclear envelope assembly at the end of mitosis in suspension-cultured Apium graveolens cells
    • Kimura Y, Kuroda C, Masuda K. 2010. Differential nuclear envelope assembly at the end of mitosis in suspension-cultured Apium graveolens cells. Chromosoma 119, 195-204.
    • (2010) Chromosoma , vol.119 , pp. 195-204
    • Kimura, Y.1    Kuroda, C.2    Masuda, K.3
  • 21
    • 0023180365 scopus 로고
    • Differential expression of nuclear lamin proteins during chicken development
    • Lehner CF, Stick R, Eppenberger HM, Nigg EA. 1987. Differential expression of nuclear lamin proteins during chicken development. Journal of Cell Biology 105, 577-587.
    • (1987) Journal of Cell Biology , vol.105 , pp. 577-587
    • Lehner, C.F.1    Stick, R.2    Eppenberger, H.M.3    Nigg, E.A.4
  • 22
    • 0033459574 scopus 로고    scopus 로고
    • Assembly and disassembly of the peripheral architecture of the plant cell nucleus during mitosis
    • Masuda K, Haruyama S, Fujino K. 1999. Assembly and disassembly of the peripheral architecture of the plant cell nucleus during mitosis. Planta 210, 165-167.
    • (1999) Planta , vol.210 , pp. 165-167
    • Masuda, K.1    Haruyama, S.2    Fujino, K.3
  • 23
    • 0000023703 scopus 로고
    • Residual structure and constituent proteins of the peripheral framework of the cell nucleus in somatic embryos from Daucus carota L
    • Masuda K, Takahashi S, Nomura K, Arimoto M, Inoue M. 1993. Residual structure and constituent proteins of the peripheral framework of the cell nucleus in somatic embryos from Daucus carota L. Planta 191, 532-540.
    • (1993) Planta , vol.191 , pp. 532-540
    • Masuda, K.1    Takahashi, S.2    Nomura, K.3    Arimoto, M.4    Inoue, M.5
  • 24
    • 0031562693 scopus 로고    scopus 로고
    • Peripheral framework of carrot cell nucleus contains a novel protein predicted to exhibit a long alpha-helical domain
    • Masuda K, Xu ZJ, Takahashi S, Ito A, Ono M, Nomura K, Inoue M. 1997. Peripheral framework of carrot cell nucleus contains a novel protein predicted to exhibit a long alpha-helical domain. Experimental Cell Research 232, 173-181.
    • (1997) Experimental Cell Research , vol.232 , pp. 173-181
    • Masuda, K.1    Xu, Z.J.2    Takahashi, S.3    Ito, A.4    Ono, M.5    Nomura, K.6    Inoue, M.7
  • 25
    • 77957678443 scopus 로고    scopus 로고
    • LINC complexes in health and disease
    • Mejat A, Misteli T. 2010. LINC complexes in health and disease. Nucleus 1, 40-52.
    • (2010) Nucleus , vol.1 , pp. 40-52
    • Mejat, A.1    Misteli, T.2
  • 27
    • 0026082690 scopus 로고
    • Isolation and ultrastructural characterization of the residual nuclear matrix in a plant cell system
    • Moreno Díaz de la Espina S, Barthellemy I, Cerezuela MA. 1991. Isolation and ultrastructural characterization of the residual nuclear matrix in a plant cell system. Chromosoma 100, 110-117.
    • (1991) Chromosoma , vol.100 , pp. 110-117
    • Moreno Díaz De La Espina, S.1    Barthellemy, I.2    Cerezuela, M.A.3
  • 28
    • 27944487517 scopus 로고    scopus 로고
    • Functional isolation of novel nuclear proteins showing a variety of subnuclear localizations
    • Moriguchi K, Suzuki T, Ito Y, Yamazaki Y, Niwa Y, Kurata N. 2005. Functional isolation of novel nuclear proteins showing a variety of subnuclear localizations. The Plant Cell 17, 389-403.
    • (2005) The Plant Cell , vol.17 , pp. 389-403
    • Moriguchi, K.1    Suzuki, T.2    Ito, Y.3    Yamazaki, Y.4    Niwa, Y.5    Kurata, N.6
  • 29
    • 78649779114 scopus 로고    scopus 로고
    • Structure and expression of the maize (Zea mays L.) SUN-domain protein gene family: Evidence for the existence of two divergent classes of SUN proteins in plants
    • Murphy SP, Simmons CR, Bass HW. 2010. Structure and expression of the maize (Zea mays L.) SUN-domain protein gene family: evidence for the existence of two divergent classes of SUN proteins in plants. BMC Plant Biology 10, 269.
    • (2010) BMC Plant Biology , vol.10 , pp. 269
    • Murphy, S.P.1    Simmons, C.R.2    Bass, H.W.3
  • 30
    • 79954565013 scopus 로고    scopus 로고
    • Dynamics of Arabidopsis SUN proteins during mitosis and their involvement in nuclear shaping
    • Oda Y, Fukuda H. 2011. Dynamics of Arabidopsis SUN proteins during mitosis and their involvement in nuclear shaping. The Plant Journal 66, 629-641.
    • (2011) The Plant Journal , vol.66 , pp. 629-641
    • Oda, Y.1    Fukuda, H.2
  • 31
    • 79551711081 scopus 로고    scopus 로고
    • Nuclear spectrin-like proteins are structural actin-binding proteins in plants
    • Perez-Munive C, Moreno Díaz de la Espina S. 2011. Nuclear spectrin-like proteins are structural actin-binding proteins in plants. Biology of the Cell 103, 145-157.
    • (2011) Biology of the Cell , vol.103 , pp. 145-157
    • Perez-Munive, C.1    Moreno Díaz De La Espina, S.2
  • 32
    • 84860138137 scopus 로고    scopus 로고
    • Evolution of the lamin protein family: What introns can tell
    • Peter A, Stick R. 2012. Evolution of the lamin protein family: what introns can tell. Nucleus 3, 44-59.
    • (2012) Nucleus , vol.3 , pp. 44-59
    • Peter, A.1    Stick, R.2
  • 35
    • 77956588049 scopus 로고    scopus 로고
    • Direct actin binding to A- and B-type lamin tails and actin filament bundling by the lamin A tail
    • Simon DN, Zastrow MS, Wilson KL. 2010. Direct actin binding to A- and B-type lamin tails and actin filament bundling by the lamin A tail. Nucleus 1, 264-272.
    • (2010) Nucleus , vol.1 , pp. 264-272
    • Simon, D.N.1    Zastrow, M.S.2    Wilson, K.L.3
  • 36
    • 79960258826 scopus 로고    scopus 로고
    • Involvement of the nuclear pore complex in morphology of the plant nucleus
    • Tamura K, Hara-Nishimura I. 2011. Involvement of the nuclear pore complex in morphology of the plant nucleus. Nucleus 2, 168-172.
    • (2011) Nucleus , vol.2 , pp. 168-172
    • Tamura, K.1    Hara-Nishimura, I.2
  • 37
    • 79957613599 scopus 로고    scopus 로고
    • MEGA5: Molecular Evolutionary Genetics Analysis using maximum likelihood, evolutionary distance, and maximum parsimony methods
    • Tamura K, Peterson D, Peterson N, Stecher G, Nei M, Kumar S. 2011. MEGA5: Molecular Evolutionary Genetics Analysis using maximum likelihood, evolutionary distance, and maximum parsimony methods. Molecular Biology and Evolution 28, 2731-2739.
    • (2011) Molecular Biology and Evolution , vol.28 , pp. 2731-2739
    • Tamura, K.1    Peterson, D.2    Peterson, N.3    Stecher, G.4    Nei, M.5    Kumar, S.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.